ID   TKT_STAAC               Reviewed;         662 AA.
AC   Q5HG77;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Transketolase;
DE            EC=2.2.1.1;
GN   Name=tkt; OrderedLocusNames=SACOL1377;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
CC   -!- FUNCTION: Catalyzes the transfer of a two-carbon ketol group from a
CC       ketose donor to an aldose acceptor, via a covalent intermediate with
CC       the cofactor thiamine pyrophosphate. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC         aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate;
CC         Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737,
CC         ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent
CC       metal cations, such as Ca(2+), Mn(2+) and Co(2+). {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
CC   -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
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DR   EMBL; CP000046; AAW36626.1; -; Genomic_DNA.
DR   RefSeq; WP_000481443.1; NC_002951.2.
DR   AlphaFoldDB; Q5HG77; -.
DR   SMR; Q5HG77; -.
DR   EnsemblBacteria; AAW36626; AAW36626; SACOL1377.
DR   KEGG; sac:SACOL1377; -.
DR   HOGENOM; CLU_009227_0_0_9; -.
DR   OMA; HHTEGIE; -.
DR   UniPathway; UPA00115; -.
DR   UniPathway; UPA00116; -.
DR   Proteomes; UP000000530; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway.
DR   CDD; cd02012; TPP_TK; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR005478; Transketolase_bac-like.
DR   InterPro; IPR020826; Transketolase_BS.
DR   InterPro; IPR033248; Transketolase_C.
DR   InterPro; IPR033247; Transketolase_fam.
DR   InterPro; IPR005474; Transketolase_N.
DR   PANTHER; PTHR43522; PTHR43522; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   Pfam; PF00456; Transketolase_N; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   SUPFAM; SSF52922; SSF52922; 1.
DR   TIGRFAMs; TIGR00232; tktlase_bact; 1.
DR   PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR   PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE   3: Inferred from homology;
KW   Calcium; DNA recombination; Magnesium; Metal-binding;
KW   Thiamine pyrophosphate; Transferase.
FT   CHAIN           1..662
FT                   /note="Transketolase"
FT                   /id="PRO_0000191870"
FT   ACT_SITE        410
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         28
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         68
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         115..117
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         156
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         157
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         186
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         186
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         188
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         261
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         261
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         356
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         383
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         436
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         460
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         468
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         519
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            28
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250"
FT   SITE            261
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   662 AA;  72251 MW;  3723932E63AFAC9C CRC64;
     MFNEKDQLAV DTLRALSIDT IEKANSGHPG LPMGAAPMAY TLWTRHLNFN PQSKDYFNRD
     RFVLSAGHGS ALLYSLLHVS GSLELEELKQ FRQWGSKTPG HPEYRHTDGV EVTTGPLGQG
     FAMSVGLALA EDHLAGKFNK EGYNVVDHYT YVLASDGDLM EGISHEAASF AGHNKLSKLV
     VLYDSNDISL DGELNKAFSE NTKARFEAYG WNYLLVKDGN DLEEIDKAIT TAKSQEGPTI
     IEVKTTIGFG SPNKAGTNGV HGAPLGEVER KLTFENYGLD PEKRFNVSEE VYEIFQNTML
     KRANEDESQW NSLLEKYAET YPELAEEFKL AISGKLPKNY KDELPRFELG HNGASRADSG
     TVIQAISKTV PSFFGGSADL AGSNKSNVND ATDYSSETPE GKNVWFGVRE FAMGAAVNGM
     AAHGGLHPYG ATFFVFSDYL KPALRLSSIM GLNATFIFTH DSIAVGEDGP THEPIEQLAG
     LRAIPNMNVI RPADGNETRV AWEVALESES TPTSLVLTRQ NLPVLDVPED VVEEGVRKGA
     YTVYGSEETP EFLLLASGSE VSLAVEAAKD LEKQGKSVRV VSMPNWNAFE QQSEEYKESV
     IPSSVTKRVA IEMASPLGWH KYVGTAGKVI AIDGFGASAP GDLVVEKYGF TKENILNQVM
     SL